PURIFICATION AND CHARACTERIZATION OF LIPASE ENZYME FROM PHASEOLUS VULGARIS (FRENCH BEAN) SEEDS AND SESAMUM INDICUM (SESAME SEEDS) AND THEIR SYNERGISTIC ACTION IN MEDICAMENTS FOR ATHEROSCLEROSIS

This study is taken for the screening of lipolytic enzymes from plant seeds to degrade the lipids by regulating several signaling proteins in the progression of atherosclerosis. Bioactive components from Phaseolus vulgaris (French bean) seeds and Sesamum indicum (sesame seeds) have been studied for their degradation properties of triglycerides and cholesterol by titration and plate assay method. The enzyme was purified to homogeneity by Ammonium sulphate fractionation at 60% saturation, with an overall yield of 26% and 1.3 fold purification. Molecular mass of is ~30 kDa. The ideal pH required for the enzyme activity was observed to be 7.0 and was stable at a pH extend 6.0 to 8.0, optimum temperature was 40°C and 100% stable even incubated for 2 h. The metal ions Ca2+, Mg2+, improved relative activity of the enzyme while EDTA and Hg2+ were hindered the enzyme activity. The molecular weight of the lipolytic proteins from Sesamum indicum and Phaseolus vulgaris showed above 30kDa. According to literature review plants based enzymes molecular weight range from 12kDa to 27kDa. Although the enzyme from plant source showed high molecular weight comparing to its usual range. Hence this lipolytic enzyme has diverse applications in pharmaceutical industry for is substrate specificity, enantioselective and with higher molecular weight.